cathepsin l

Cathepsin L is a biochemical reagent, utilized as a biomaterial or organic compound in life sciences research.

L-Arginine-7-amido-4-methylcoumarin hydrochloride is a specific fluorescent substrate and activity assay reagent for cathepsin H, and also serves as a substrate for the amino acid protease AP II.

L-Arginine p-nitroanilide dihydrochloride, 98% (H-Arg-pNA 2HCl, 98%), serves as a chromogenic substrate for cathepsin H and aminopeptidase.

L-Arginine 7-amido-4-methylcoumarin dihydrochloride is a specialized fluorescent substrate with potential for detecting cathepsin H activity. It provides a high-sensitivity fluorescent signal for biological research and holds significant application in enzyme activity assays.

Alloc-Val-Ala-OH (((Allyloxy)carbonyl)-L-valyl-L-alanine) serves as a building block in the synthesis of Tesirine, which is a clinical antibody-drug conjugate (ADC) featuring a pyrrolobenzodiazepine (PBD) dimer payload. The Val-Ala sequence is cleaved specifically by cathepsin B. The Alloc group is stable towards piperidine and TFA, yet can be easily removed under mild conditions via palladium-catalyzed allyl transfer.